The amino acid sequence of the light chain of Acanthamoeba myosin IC
Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed t...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
WANG, ZHEN-YUAN [verfasserIn] |
|---|
| Format: |
Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1997 |
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| Schlagwörter: |
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| Anmerkung: |
© Chapman and Hall 1997 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of muscle research and cell motility - Kluwer Academic Publishers, 1980, 18(1997), 3 vom: Mai, Seite 395-398 |
|---|---|
| Übergeordnetes Werk: |
volume:18 ; year:1997 ; number:3 ; month:05 ; pages:395-398 |
| Links: |
|---|
| DOI / URN: |
10.1023/A:1018686428955 |
|---|
| Katalog-ID: |
OLC2067120867 |
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| 245 | 1 | 0 | |a The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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| 520 | |a Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin | ||
| 650 | 4 | |a Molecular Weight | |
| 650 | 4 | |a Amino Acid Sequence | |
| 650 | 4 | |a Phylogenetic Analysis | |
| 650 | 4 | |a Light Chain | |
| 650 | 4 | |a cDNA Sequence | |
| 700 | 1 | |a SAKAI, JUN |4 aut | |
| 700 | 1 | |a MATSUDAIRA, PAUL T. |4 aut | |
| 700 | 1 | |a BAINES, IVAN C. |4 aut | |
| 700 | 1 | |a SELLERS, JAMES R. |4 aut | |
| 700 | 1 | |a HAMMER III, JOHN A. |4 aut | |
| 700 | 1 | |a KORN, EDWARD D. |4 aut | |
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10.1023/A:1018686428955 doi (DE-627)OLC2067120867 (DE-He213)A:1018686428955-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid WANG, ZHEN-YUAN verfasserin aut The amino acid sequence of the light chain of Acanthamoeba myosin IC 1997 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall 1997 Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin Molecular Weight Amino Acid Sequence Phylogenetic Analysis Light Chain cDNA Sequence SAKAI, JUN aut MATSUDAIRA, PAUL T. aut BAINES, IVAN C. aut SELLERS, JAMES R. aut HAMMER III, JOHN A. aut KORN, EDWARD D. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 18(1997), 3 vom: Mai, Seite 395-398 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:18 year:1997 number:3 month:05 pages:395-398 https://doi.org/10.1023/A:1018686428955 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 18 1997 3 05 395-398 |
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10.1023/A:1018686428955 doi (DE-627)OLC2067120867 (DE-He213)A:1018686428955-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid WANG, ZHEN-YUAN verfasserin aut The amino acid sequence of the light chain of Acanthamoeba myosin IC 1997 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall 1997 Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin Molecular Weight Amino Acid Sequence Phylogenetic Analysis Light Chain cDNA Sequence SAKAI, JUN aut MATSUDAIRA, PAUL T. aut BAINES, IVAN C. aut SELLERS, JAMES R. aut HAMMER III, JOHN A. aut KORN, EDWARD D. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 18(1997), 3 vom: Mai, Seite 395-398 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:18 year:1997 number:3 month:05 pages:395-398 https://doi.org/10.1023/A:1018686428955 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 18 1997 3 05 395-398 |
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10.1023/A:1018686428955 doi (DE-627)OLC2067120867 (DE-He213)A:1018686428955-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid WANG, ZHEN-YUAN verfasserin aut The amino acid sequence of the light chain of Acanthamoeba myosin IC 1997 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall 1997 Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin Molecular Weight Amino Acid Sequence Phylogenetic Analysis Light Chain cDNA Sequence SAKAI, JUN aut MATSUDAIRA, PAUL T. aut BAINES, IVAN C. aut SELLERS, JAMES R. aut HAMMER III, JOHN A. aut KORN, EDWARD D. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 18(1997), 3 vom: Mai, Seite 395-398 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:18 year:1997 number:3 month:05 pages:395-398 https://doi.org/10.1023/A:1018686428955 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 18 1997 3 05 395-398 |
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10.1023/A:1018686428955 doi (DE-627)OLC2067120867 (DE-He213)A:1018686428955-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid WANG, ZHEN-YUAN verfasserin aut The amino acid sequence of the light chain of Acanthamoeba myosin IC 1997 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman and Hall 1997 Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin Molecular Weight Amino Acid Sequence Phylogenetic Analysis Light Chain cDNA Sequence SAKAI, JUN aut MATSUDAIRA, PAUL T. aut BAINES, IVAN C. aut SELLERS, JAMES R. aut HAMMER III, JOHN A. aut KORN, EDWARD D. aut Enthalten in Journal of muscle research and cell motility Kluwer Academic Publishers, 1980 18(1997), 3 vom: Mai, Seite 395-398 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:18 year:1997 number:3 month:05 pages:395-398 https://doi.org/10.1023/A:1018686428955 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2021 GBV_ILN_2219 GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4082 GBV_ILN_4219 AR 18 1997 3 05 395-398 |
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WANG, ZHEN-YUAN |
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WANG, ZHEN-YUAN ddc 590 ssgn 12 fid BIODIV misc Molecular Weight misc Amino Acid Sequence misc Phylogenetic Analysis misc Light Chain misc cDNA Sequence The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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590 570 VZ 12 ssgn BIODIV DE-30 fid The amino acid sequence of the light chain of Acanthamoeba myosin IC Molecular Weight Amino Acid Sequence Phylogenetic Analysis Light Chain cDNA Sequence |
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ddc 590 ssgn 12 fid BIODIV misc Molecular Weight misc Amino Acid Sequence misc Phylogenetic Analysis misc Light Chain misc cDNA Sequence |
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ddc 590 ssgn 12 fid BIODIV misc Molecular Weight misc Amino Acid Sequence misc Phylogenetic Analysis misc Light Chain misc cDNA Sequence |
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The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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WANG, ZHEN-YUAN |
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Journal of muscle research and cell motility |
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Journal of muscle research and cell motility |
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WANG, ZHEN-YUAN SAKAI, JUN MATSUDAIRA, PAUL T. BAINES, IVAN C. SELLERS, JAMES R. HAMMER III, JOHN A. KORN, EDWARD D. |
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the amino acid sequence of the light chain of acanthamoeba myosin ic |
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The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin © Chapman and Hall 1997 |
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Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin © Chapman and Hall 1997 |
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Abstract The amino acid sequence of the light chain of Acanthamoebamyosin IC deduced from the cDNA sequence comprises 149 aminoacids with a calculated molecular weight of 16739. All but the 3N-terminal residues were also determined by amino acid sequencingof the purified protein, which also showed the N-terminus to beblocked. Phylogenetic analysis shows Acanthamoeba myosin IC lightchain to be more similar to the calmodulin subfamily of EF-handcalcium-modulated proteins than to the myosin II essential lightchain or regulatory light chain subfamilies. In pairwisecomparisons, the myosin IC light chain sequence is most similarto sequences of calmodulins (∼50% identical) and a squidcalcium-binding protein (∼43% identical); the sequence is∼37% identical to the calcium-binding essential light chainof Physarum myosin II and ∼30% identical to the essentiallight chain of Acanthamoeba myosin II, and the essential lightchain and regulatory light chain of Dictyostelium myosin II. Thesequence predicts four helix-loop-helix domains with possiblecalcium-binding sites in domains I and III, suggesting thatcalcium may affect the activity of this unconventional myosin.This is the first report of the sequence of an unconventionalmyosin light chain other than calmodulin © Chapman and Hall 1997 |
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The amino acid sequence of the light chain of Acanthamoeba myosin IC |
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